LIPIDAT: a database of lipid phase transition temperatures and enthalpy changes. DMPC data subset analysis.

The systematic study of the mesomorphic phase properties of synthetic and biologically derived lipids began some 30 years ago. In the past decade, interest in this area has grown enormously. As a result, there exists a wealth of information on lipid phase behavior, but unfortunately these data have until now been scattered throughout the literature in a variety of books, proceedings and journals. The data have recently been compiled in a centralized database, LIPIDAT, with a view to providing ready access to the data and to the appropriate literature. LIPIDAT consists of a tabulation of all known mesomorphic and polymorphic phase transition temperatures and enthalpy changes for synthetic and biologically-derived lipids in the dry and in the partially and fully hydrated states. Also included is the effect of pH, and of salt and metal ion concentration and other additives such as proteins, drugs, etc., on the thermodynamic values. The methods used in making the measurements and the experimental conditions are reported. Bibliographic information includes comprehensive literature referencing and list of authors, but does not at the present time include article titles. As of this writing, the database is current through June, 1990 and is approaching 10,000 records in length. Each record contains 28 fields. In this paper we report the contents and present an analysis of LIPIDAT as it refers to fully hydrated 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC). This database subset represents about 7% of all LIPIDAT records. It includes data collected over a 23-year period from 1967 to 1989 and consists of 702 records obtained from 336 articles in 55 different journals. The number of records per year rises steadily beginning in 1971, reaches a maximum of 89 records/year in 1977 and remains relatively constant at 60-70 records/year in the succeeding period. Journals making the greatest contribution to the DMPC subset include Biochimica et Biophysica Acta, Biochemistry, Chemistry and Physics of Lipids and the Biophysical Journal. These four journals account for 71% of the total records in the database subset. The analysis shows that differential scanning calorimetry, electron spin resonance, fluorescence, nuclear magnetic resonance and Raman spectroscopy are the methods most commonly used for DMPC transition temperature determination. An interesting pattern emerges as to the place in time the different methods assume or loose popularity.(ABSTRACT TRUNCATED AT 400 WORDS)     

Genome-wide CRISPR Screens Reveal Host Factors Critical for SARS-CoV-2 Infection

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Environmentally constrained mutation and adaptive evolution in Salmonella

The relationship between environment and mutation is complex [1]. Claims of Lamarkian mutation [2] have proved unfounded [3], [4] and [5]; it is apparent, however, that the external environment can influence the generation of heritable variation, through either direct effects on DNA sequence [6] or DNA maintenance and copying mechanisms [7], [8], [9] and [10], or as a consequence of evolutionary processes [11], [12], [13], [14], [15] and [16]. The spectrum of mutational events subject to environmental influence is unknown [6] and precisely how environmental signals modulate mutation is unclear. Evidence from bacteria suggests that a transient recombination-dependent hypermutational state can be induced by starvation [5]. It is also apparent that chnages in the mutability of specific loci can be influenced by alterations in DNA topology [10] and [17]. Here we describe a remarkable instance of adaptive evolution in Salmonella which is caused by a mutation that occurs in intermediate-strength osmotic environments. We show that the mutation is not ‘directed’ and describe its genetic basis. We also present compelling evidence in support of the hypothesis that the mutational event is constrained by signals transmitted from the external environment via changes in the activity of DNA gyrase.     

Galectin 9 is the sugar-regulated urate transporter/channel UAT

UAT, also designated galectin 9, is a multifunctional protein that can function as a urate channel/transporter, a regulator of thymocyte-epithelial cell interactions, a tumor antigen, an eosinophil chemotactic factor, and a mediator of apoptosis. We review the evidence that UAT is a transmembrane protein that transports urate, describe our molecular model for this protein, and discuss the evidence from epitope tag and lipid bilayer studies that support this model of the transporter. The properties of recombinant UAT are compared with those of urate transport into membrane vesicles derived from proximal tubule cells in rat kidney cortex. In addition, we review channel functions predicted by our molecular model that resulted in the novel finding that the urate channel activity is regulated by sugars and adenosine. Finally, the presence and possible functions of at least 4 isoforms of UAT and a closely related gene hUAT2 are discussed. Published in 2004.     

Pinocytic uptake and intracellular degradation of N-(2-hydroxypropyl)methacrylamide copolymers a potential drug delivery system

Synthetic ¹²⁵I-labelled N-(2-hydroxypropyl)methacrylamide copolymers containing four different, potentially degradable peptidyl side chains were incubated with rat visceral yolk sacs cultured in vitro. All copolymers were captured by fluid-phase pinocytosis and three of the side chains were susceptible to lysosomal hydrolysis, resulting in release of [¹²⁵I]iodotyrosine back into the culture medium. Uptake and degradation was completely inhibited by 2,4-dinitrophenol. The thiol-proteinase inhibitor leupeptin did not affect the rate of pinocytosis, but caused different degrees of inhibition of hydrolysis depending on side chain composition.